2H6C

Crystal structure of reduced CprK in absence of any ligand

2H6C の概要

• エントリーDOI: 10.2210/pdb2h6c/pdb
• 関連するPDBエントリー: 2H6B
• 分子名称: ChloroPhenol Reduction gene K (1 entity in total)
• 機能のキーワード: dna binding, helix-turn-helix, chlorophenol, halorespiration, cprk, dna binding protein
• 由来する生物種: Desulfitobacterium dehalogenans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53355.45

構造登録者

Levy, C.,Leys, D. (登録日: 2006-05-31, 公開日: 2006-07-04, 最終更新日: 2023-08-30)

主引用文献

Joyce, M.G.,Levy, C.,Pop, S.M.,Biehl, B.D.,Doukov, T.I.,Ryter, J.M.,Mazon, H.,Smidt, H.,van den Heuvel, R.H.,Ragsdale, S.W.,van der Oost, J.,Leys, D.
CprK Crystal Structures Reveal Mechanism for Transcriptional Control of Halorespiration.
J.Biol.Chem., 281:28318-28325, 2006

PubMed Abstract: Halorespiration is a bacterial respiratory process in which haloorganic compounds act as terminal electron acceptors. This process is controlled at transcriptional level by CprK, a member of the ubiquitous CRP-FNR family. Here we present the crystal structures of oxidized CprK in presence of the ligand ortho-chlorophenolacetic acid and of reduced CprK in absence of this ligand. These structures reveal that highly specific binding of chlorinated, rather than the corresponding non-chlorinated, phenolic compounds in the NH(2)-terminal beta-barrels causes reorientation of these domains with respect to the central alpha-helix at the dimer interface. Unexpectedly, the COOH-terminal DNA-binding domains dimerize in the non-DNA binding state. We postulate the ligand-induced conformational change allows formation of interdomain contacts that disrupt the DNA domain dimer interface and leads to repositioning of the helix-turn-helix motifs. These structures provide a structural framework for further studies on transcriptional control by CRP-FNR homologs in general and of halorespiration regulation by CprK in particular.

PubMed: 16803881
DOI: 10.1074/jbc.M602654200

実験手法

X-RAY DIFFRACTION (2.9 Å)